Molecular cloning and characterization of mouse ficolin-A

Biochem Biophys Res Commun. 1998 Mar 27;244(3):796-800. doi: 10.1006/bbrc.1998.8344.

Abstract

A novel ficolin-related gene was isolated from the mouse liver lambda ZAPII cDNA library. The protein encoded by this gene consists of both collagen- and fibrinogen-like domains, which are common features of the ficolin family, and was named mouse ficolin-A. The amino acid sequence of mouse ficolin-A is 60.2, 59.8, 59.8, and 59.6% identical to those of porcine ficolin-alpha, -beta, human ficolin-1, and EBP-37/P35, respectively. Northern blot analysis showed that mRNA of mouse ficolin-A is highly expressed in liver and spleen. Immunoblot analysis using an anti-mouse ficolin-A antiserum showed that mouse ficolin-A is a plasma protein with binding activity to elastin and GlcNAc.

MeSH terms

  • Acetylglucosamine / blood
  • Acetylglucosamine / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blood Proteins / genetics*
  • Blood Proteins / metabolism
  • Carrier Proteins / blood
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Collagen / genetics
  • DNA, Complementary / genetics
  • Elastin / blood
  • Elastin / metabolism
  • Fibrinogen / genetics
  • Ficolins
  • Lectins*
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Tissue Distribution

Substances

  • Blood Proteins
  • Carrier Proteins
  • DNA, Complementary
  • Lectins
  • Fibrinogen
  • Collagen
  • Elastin
  • Acetylglucosamine

Associated data

  • GENBANK/AB007813